@-Tide peptidomimetics in water: Quantification of amino acid side chain-side chain interactions and amino acid conformational preferences in small, stabilized b-hairpins

ORGN 521

Scott T. Phillips and Paul A. Bartlett. Department of Chemistry, University of California, Berkeley, CA 94720

We have recently designed a b-strand peptidomimetic (termed an @-tide) derived from alternating azacyclohexenone units (@-units) and amino acids. These @-tides can dimerize in organic solvents and can template linked peptides into b-sheets. We now show that @-tides stabilize small b-hairpins in buffered aqueous solvent – so much so that we observe hairpins in 100% b-sheet population. In addition, we have devised a rapid circular dichroism assay based on the @-unit absorbance that allows us to quantify amino acid side chain-side chain interactions and amino acid conformational preferences for the b-sheet structure. The results and implications of these studies will be presented.

Bioorganic, Molecular Recognition, Asymmetric Reactions and Syntheses 11:00 AM-1:00 PM, Wednesday, September 10, 2003 Javits Convention Center -- Hall 1B/1C, Poster Sci-Mix 8:00 PM-10:00 PM, Monday, September 8, 2003 Javits Convention Center -- North Pavillion, Sci-Mix Division of Organic Chemistry The 226th ACS National Meeting, New York, NY, September 7-11, 2003